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Database: UniProt
Entry: A0A0M9YXF7_9ACTN
LinkDB: A0A0M9YXF7_9ACTN
Original site: A0A0M9YXF7_9ACTN 
ID   A0A0M9YXF7_9ACTN        Unreviewed;       442 AA.
AC   A0A0M9YXF7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=ADK57_06275 {ECO:0000313|EMBL:KOU75980.1};
OS   Streptomyces sp. MMG1533.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU75980.1, ECO:0000313|Proteomes:UP000037741};
RN   [1] {ECO:0000313|Proteomes:UP000037741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|RuleBase:RU361174}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOU75980.1}.
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DR   EMBL; LGDG01000028; KOU75980.1; -; Genomic_DNA.
DR   RefSeq; WP_053748336.1; NZ_LGDG01000028.1.
DR   AlphaFoldDB; A0A0M9YXF7; -.
DR   STRING; 1415546.ADK57_06275; -.
DR   PATRIC; fig|1415546.3.peg.1376; -.
DR   OrthoDB; 9815836at2; -.
DR   Proteomes; UP000037741; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037741};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:KOU75980.1}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..442
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005841947"
FT   DOMAIN          27..330
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          337..442
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   ACT_SITE        264
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   442 AA;  46300 MW;  84E6B4A0357EFEC9 CRC64;
     MVTRTSIRLG MASLLAIAGL TALSAPADAA STLGAAAAEK GRYFGAAVAA NHLGESAYVS
     TLDTEFNSVT PENEMKWDAV ESTRNSFNFT AADQIVSHAQ SKGMKVRGHT LVWHSQLPSW
     VGTLAAADLR TAMNNHINQV MGHYKGKIHS WDVVNEAFQD GSSGARRSSP FQDKLGNGFI
     EEAFRTARAA DPAAKLCYND YNTDGVNAKS TAVYNLVKDF KARGVPIDCV GFQSHFNSAS
     PVPSDYQANL QRFADLGVDV QITELDIEGS GTSQATSYSN VVKACLAVSR CTGITVWGVT
     DKYSWRAGGT PLLFDGNYSK KAAYTAVLTA LGGTGSGGGG TAACSVSYSK QEEWSDRFNG
     KVTVTAGGSA ISNWTTTVTV TSPQKISATW NGTPTWDSSG NVMTMKPNGN GSLAAGASTS
     FGFTVMTNGN TAAPVLGSCT AS
//
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